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Database: UniProt
Entry: A0A0P1BYY5_9CYAN
LinkDB: A0A0P1BYY5_9CYAN
Original site: A0A0P1BYY5_9CYAN 
ID   A0A0P1BYY5_9CYAN        Unreviewed;       115 AA.
AC   A0A0P1BYY5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   31-JAN-2018, entry version 10.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE            EC=1.6.5.- {ECO:0000256|HAMAP-Rule:MF_01352};
DE   AltName: Full=NAD(P)H dehydrogenase I subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE            Short=NDH-1 subunit M {ECO:0000256|HAMAP-Rule:MF_01352};
DE            Short=NDH-M {ECO:0000256|HAMAP-Rule:MF_01352};
GN   Name=ndhM {ECO:0000256|HAMAP-Rule:MF_01352};
GN   ORFNames=apha_02210 {ECO:0000313|EMBL:CEJ45902.1};
OS   Chrysosporum ovalisporum.
OC   Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Chrysosporum.
OX   NCBI_TaxID=75695 {ECO:0000313|EMBL:CEJ45902.1, ECO:0000313|Proteomes:UP000051809};
RN   [1] {ECO:0000313|EMBL:CEJ45902.1, ECO:0000313|Proteomes:UP000051809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAM-MAO {ECO:0000313|EMBL:CEJ45902.1,
RC   ECO:0000313|Proteomes:UP000051809};
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor,
CC       via FMN and iron-sulfur (Fe-S) centers, to quinones in the
CC       respiratory and/or the photosynthetic chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       plastoquinone. Couples the redox reaction to proton translocation,
CC       and thus conserves the redox energy in a proton gradient.
CC       Cyanobacterial NDH-1 also plays a role in inorganic carbon-
CC       concentration. {ECO:0000256|HAMAP-Rule:MF_01352}.
CC   -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
CC       plastoquinol. {ECO:0000256|HAMAP-Rule:MF_01352}.
CC   -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC       different subcomplexes with different compositions have been
CC       identified which probably have different functions.
CC       {ECO:0000256|HAMAP-Rule:MF_01352}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_01352}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_01352}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_01352}.
CC   -!- SIMILARITY: Belongs to the complex I NdhM subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01352}.
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DR   EMBL; CDHJ01000149; CEJ45902.1; -; Genomic_DNA.
DR   EnsemblBacteria; CEJ45902; CEJ45902; apha_02210.
DR   Proteomes; UP000051809; Unassembled WGS sequence.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01352; NDH1_NDH1M; 1.
DR   InterPro; IPR018922; NdhM.
DR   PANTHER; PTHR36900; PTHR36900; 1.
DR   Pfam; PF10664; NdhM; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000051809};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01352};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01352};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051809};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01352};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01352}.
SQ   SEQUENCE   115 AA;  13150 MW;  8269D9DF5E66253D CRC64;
     MLLKSTTRHI RIFAAEIDRD GELIPSNQVL TLDVDPDNEF NWNEDALQKV YRQFDQLVEA
     SSGADLTDYN LRRMGSDLEH YLRSLLQKGE ISYNLSGRVA NYSMGLPQVV ADENE
//
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